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P21550

- ENOB_MOUSE

UniProt

P21550 - ENOB_MOUSE

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Protein

Beta-enolase

Gene
Eno3, Eno-3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Appears to have a function in striated muscle development and regeneration.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581Substrate By similarity
Binding sitei167 – 1671Substrate By similarity
Active sitei210 – 2101Proton donor By similarity
Metal bindingi245 – 2451Magnesium By similarity
Metal bindingi293 – 2931Magnesium By similarity
Binding sitei293 – 2931Substrate By similarity
Metal bindingi318 – 3181Magnesium By similarity
Binding sitei318 – 3181Substrate By similarity
Active sitei343 – 3431Proton acceptor By similarity
Binding sitei394 – 3941Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphopyruvate hydratase activity Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. glycolytic process Source: UniProtKB-UniPathway
  3. response to drug Source: Ensembl
  4. skeletal muscle tissue regeneration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.11. 3474.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name:
MSE
Skeletal muscle enolase
Gene namesi
Name:Eno3
Synonyms:Eno-3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:95395. Eno3.

Subcellular locationi

Cytoplasm
Note: Localized to the Z line. Some colocalization with CKM at M-band By similarity.1 Publication

GO - Cellular componenti

  1. membrane Source: Ensembl
  2. phosphopyruvate hydratase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 434433Beta-enolaseUniRule annotationPRO_0000134108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21550.
PaxDbiP21550.
PRIDEiP21550.

2D gel databases

SWISS-2DPAGEP21550.
UCD-2DPAGEP21550.

PTM databases

PhosphoSiteiP21550.

Expressioni

Tissue specificityi

The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I.1 Publication

Developmental stagei

During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In hindleg muscle, first expressed at E15 after which, levels increase sharply between E15 and E17. A steep prenatal rise in expression accompanies the formation of secondary myofibers and the development of innervation. High levels continue throughout newborn and adult stages. Beginning at postnatal day 5, a second sharp increase in expression correlates with the definitive specialization of the myofibers. Later in development, mainly expressed in fast-twitch fibers. In cardiac muscle, first expressed in the embryo in the cardiac tube.2 Publications

Inductioni

Levels decrease in degenerating myofibers, and increase with their regeneration.1 Publication

Gene expression databases

ArrayExpressiP21550.
BgeeiP21550.
CleanExiMM_ENO3.
GenevestigatoriP21550.

Interactioni

Subunit structurei

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD By similarity.1 Publication

Protein-protein interaction databases

BioGridi199453. 2 interactions.
IntActiP21550. 4 interactions.
MINTiMINT-1855839.

Structurei

3D structure databases

ProteinModelPortaliP21550.
SMRiP21550. Positions 1-434.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate binding By similarity

Sequence similaritiesi

Belongs to the enolase family.

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP21550.
KOiK01689.
OMAiGELYKNF.
PhylomeDBiP21550.
TreeFamiTF300391.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21550-1 [UniParc]FASTAAdd to Basket

« Hide

MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR    50
DGDKARYLGK GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT 100
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLVLPVPAF 150
NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY 200
GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE 250
FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD 300
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV 350
TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
SERLAKYNQL MRIEEALGDK AVFAGRKFRN PKAK 434
Length:434
Mass (Da):47,025
Last modified:January 23, 2007 - v3
Checksum:iA1F757D83709D2B8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2352AG → NA in AAA37554. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61600 Genomic DNA. Translation: CAA43797.1.
X57747 mRNA. Translation: CAA40913.1.
X62667 mRNA. Translation: CAA44540.1.
AK002485 mRNA. Translation: BAB22137.1.
BC013460 mRNA. Translation: AAH13460.1.
M20745 mRNA. Translation: AAA37554.1.
CCDSiCCDS24961.1.
PIRiS17109. NOMSB.
RefSeqiNP_001129534.1. NM_001136062.2.
NP_001263214.1. NM_001276285.1.
NP_031959.1. NM_007933.3.
XP_006532225.1. XM_006532162.1.
XP_006537193.1. XM_006537130.1.
UniGeneiMm.251322.
Mm.491763.

Genome annotation databases

EnsembliENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600.
ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600.
ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600.
GeneIDi13808.
KEGGimmu:13808.
UCSCiuc007jvx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61600 Genomic DNA. Translation: CAA43797.1 .
X57747 mRNA. Translation: CAA40913.1 .
X62667 mRNA. Translation: CAA44540.1 .
AK002485 mRNA. Translation: BAB22137.1 .
BC013460 mRNA. Translation: AAH13460.1 .
M20745 mRNA. Translation: AAA37554.1 .
CCDSi CCDS24961.1.
PIRi S17109. NOMSB.
RefSeqi NP_001129534.1. NM_001136062.2.
NP_001263214.1. NM_001276285.1.
NP_031959.1. NM_007933.3.
XP_006532225.1. XM_006532162.1.
XP_006537193.1. XM_006537130.1.
UniGenei Mm.251322.
Mm.491763.

3D structure databases

ProteinModelPortali P21550.
SMRi P21550. Positions 1-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199453. 2 interactions.
IntActi P21550. 4 interactions.
MINTi MINT-1855839.

PTM databases

PhosphoSitei P21550.

2D gel databases

SWISS-2DPAGE P21550.
UCD-2DPAGE P21550.

Proteomic databases

MaxQBi P21550.
PaxDbi P21550.
PRIDEi P21550.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072841 ; ENSMUSP00000072620 ; ENSMUSG00000060600 .
ENSMUST00000108548 ; ENSMUSP00000104188 ; ENSMUSG00000060600 .
ENSMUST00000170716 ; ENSMUSP00000128714 ; ENSMUSG00000060600 .
GeneIDi 13808.
KEGGi mmu:13808.
UCSCi uc007jvx.2. mouse.

Organism-specific databases

CTDi 2027.
MGIi MGI:95395. Eno3.

Phylogenomic databases

eggNOGi COG0148.
GeneTreei ENSGT00550000074560.
HOGENOMi HOG000072174.
HOVERGENi HBG000067.
InParanoidi P21550.
KOi K01689.
OMAi GELYKNF.
PhylomeDBi P21550.
TreeFami TF300391.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BRENDAi 4.2.1.11. 3474.

Miscellaneous databases

NextBioi 284592.
PROi P21550.
SOURCEi Search...

Gene expression databases

ArrayExpressi P21550.
Bgeei P21550.
CleanExi MM_ENO3.
Genevestigatori P21550.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPi MF_00318. Enolase.
InterProi IPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view ]
PANTHERi PTHR11902. PTHR11902. 1 hit.
Pfami PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001400. Enolase. 1 hit.
PRINTSi PR00148. ENOLASE.
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsi TIGR01060. eno. 1 hit.
PROSITEi PS00164. ENOLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Lamande N., Brosset S., Keller A., Lucas M., Lazar M.
    Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: BALB/c and Swiss Webster.
    Tissue: Liver and Skeletal muscle.
  2. "Beta-enolase is a marker of human myoblast heterogeneity prior to differentiation."
    Peterson C.A., Cho M., Rastinejad F., Blau H.M.
    Dev. Biol. 151:626-629(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  5. Lubec G., Kang S.U., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-50; 104-120; 257-262; 336-358 AND 373-394, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression."
    Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F., Legault-Demare L., Lazar M.
    Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
  7. "Activation of the gene encoding the glycolytic enzyme beta-enolase during early myogenesis precedes an increased expression during fetal muscle development."
    Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M., Lazar M.
    Mech. Dev. 38:41-54(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVATION DURING MYOGENESIS.
  8. "Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy."
    Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.
    Am. J. Physiol. 269:H1843-H1851(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  9. "Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins."
    Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.
    Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
  10. "Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle."
    Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.
    Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Differential modulation of alpha, beta and gamma enolase isoforms in regenerating mouse skeletal muscle."
    Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H., Keller A.
    Eur. J. Biochem. 267:3735-3743(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION REGULATION.

Entry informationi

Entry nameiENOB_MOUSE
AccessioniPrimary (citable) accession number: P21550
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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